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Protein Page:
TIMP2 (human)

TIMP2 Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19. Interacts (via the C-terminal) with MMP2 (via the C- terminal PEX domain); the interaction inhibits the MMP2 activity. Down-regulated by TGFB1. Belongs to the protease inhibitor I35 (TIMP) family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Cell development/differentiation; Secreted, signal peptide; Extracellular matrix; Inhibitor protein; Secreted
Cellular Component: extracellular space; cell surface; growth cone; cell soma; extracellular region; basement membrane
Molecular Function: integrin binding; metalloendopeptidase inhibitor activity; protein binding; metal ion binding; enzyme activator activity
Biological Process: response to drug; regulation of Rap protein signal transduction; negative regulation of proteolysis; extracellular matrix organization and biogenesis; central nervous system development; negative regulation of cell proliferation; extracellular matrix disassembly; positive regulation of MAPKKK cascade; response to cytokine stimulus; negative regulation of Ras protein signal transduction; negative regulation of mitotic cell cycle; positive regulation of adenylate cyclase activity; positive regulation of neuron differentiation; aging
Reference #:  P16035 (UniProtKB)
Alt. Names/Synonyms: CSC-21K; metalloproteinase inhibitor 2; TIMP2; tissue inhibitor of metalloproteinase 2
Gene Symbols: TIMP2
Molecular weight: 24,399 Da
Basal Isoelectric point: 7.46  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

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